ID M1EPF5_MUSPF Unreviewed; 625 AA.
AC M1EPF5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Carnitine acetyltransferase {ECO:0000313|EMBL:AER96687.1};
DE Flags: Fragment;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AER96687.1};
RN [1] {ECO:0000313|EMBL:AER96687.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AER96687.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR EMBL; JP008090; AER96687.1; -; mRNA.
DR AlphaFoldDB; M1EPF5; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR PANTHER; PTHR22589:SF50; CARNITINE O-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 38..609
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT BINDING 419
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 423..430
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 454
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 456
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 465
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 504
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 555
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AER96687.1"
FT NON_TER 625
FT /evidence="ECO:0000313|EMBL:AER96687.1"
SQ SEQUENCE 625 AA; 70543 MW; 8A4EC137A999830A CRC64;
MLAFAARTVV KPLSFLKPSS LVKVSGRFKA HQDSLPRLPV PALHQSLDRY LKALQPIVSE
EEWTQTKQLV EEFQAAGGVG ERLQKGLERR ARKTENWLSE WWLKTAYLQY RQPLVIYSSP
GVALPKQDFV DLQGQLRFAA KFIEGVLDFK AMVDNETLPV EYLGGKPLCM NQYYQILSSC
RVPGPKQDTV ISFSKTKKPP MHITVVHNYQ FFELDVYHSD GTPLTSDQIF VQLEKIWNSS
LQTNKEPVGI LTSNHRNSWA KAYSTLIKDK VNRESVRSIQ KSIFTLCLDA PMPRVSEDVY
RSHVAGQMLH GGGSKLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP IIALVDHVIE
FTKKPELVRS PMVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDVV VLVFHHFGKD
FPKSEKLSPD AFVQMALQLA YYRIYKQACA TYESASLRMF HLGRTDTIRS ASVDSLAFVK
AMDDPSVSEH QKVELLRKAV QAHRAYTDQA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD
TSYAIAMHFN LSTSQVPAKT DCVMFFGPVV PDGYGICYNP MEAHINFSVS AYNSCAETNA
ARLAHYLEKA LLDMRALLQS HPRAK
//
